iga1 การใช้

• A recently advanced theory focuses on abnormalities of the IgA1 molecule.
• Thus, the IgA protease act by cleaving the proline-rich hinge region of the heavy chain of IgA1.
• IgA has two subclasses ( IgA1 and IgA2 ) and can be produced as a monomeric as well as a dimeric form.
• This strongly suggests degalactosylation of IgA1 is a result of an underlying phenomenon ( abnormal mucosal antigen handling ) and not the ultimate cause of IgA nephropathy.
• It has pneumococcal surface proteins that inhibit complement-mediated opsonization, and it secretes IgA1 protease that will destroy secretory IgA produced by the body and mediates its attachment to respiratory mucosa.
• IgA1 is one of the two immunoglobulin subclasses ( the other is IgD ) that is O-glycosylated on a number of serine and threonine residues in a special proline-rich hinge region.
• Prevailing evidence suggests that both galactose-deficient o-glycans in the hinge region of IgA1 and synthesis and binding of antibodies against IgA1 are required for immunoglobulin complexes to form and accumulate in glomeruli.
• Prevailing evidence suggests that both galactose-deficient o-glycans in the hinge region of IgA1 and synthesis and binding of antibodies against IgA1 are required for immunoglobulin complexes to form and accumulate in glomeruli.
• However, human studies have found that degalactosylation of IgA1 occurs in patients with IgA nephropathy in response only to gut antigen exposures ( not systemic ), and occurs in healthy people to a lesser extent.
• Remarkably, the IgA1 that accumulates in the kidney does not appear to originate from the mucosa-associated lymphoid tissue ( MALT ), which is the site of most upper respiratory tract infections, but from the bone marrow.